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蛋白质岩藻糖基转移酶：哺乳动物中的生物学功能与分子机制

Protein -Fucosyltransferases: Biological Functions and Molecular Mechanisms in Mammals.

作者信息

Hao Huilin, Eberand Benjamin M, Larance Mark, Haltiwanger Robert S

机构信息

Complex Carbohydrate Research Center, University of Georgia, Athens, GA 30605, USA.

Charles Perkins Centre, School of Medical Sciences, Faculty of Medicine and Health, The University of Sydney, Sydney, NSW 2006, Australia.

出版信息

Molecules. 2025 Mar 26;30(7):1470. doi: 10.3390/molecules30071470.

DOI:10.3390/molecules30071470
PMID:40286076
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11990869/
Abstract

Domain-specific -fucosylation is an unusual type of glycosylation, where the fucose is directly attached to the serine or threonine residues in specific protein domains via an -linkage. -fucosylated proteins play critical roles in a wide variety of biological events and hold important therapeutic values, with the most studied being the Notch receptors and ADAMTS proteins. -fucose glycans modulate the function of the proteins they modify and are closely associated with various diseases including cancer. In mammals, alongside the well-documented protein -fucosyltransferase (POFUT) 1-mediated -fucosylation of epidermal growth factor-like (EGF) repeats and POFUT2-mediated -fucosylation of thrombospondin type 1 repeats (TSRs), a new type of -fucosylation was recently identified on elastin microfibril interface (EMI) domains, mediated by POFUT3 and POFUT4 (formerly FUT10 and FUT11). In this review, we present an overview of our current knowledge of -fucosylation, integrating the latest findings and with a particular focus on its biological functions and molecular mechanisms.

摘要

结构域特异性岩藻糖基化是一种不寻常的糖基化类型，其中岩藻糖通过α-连接直接连接到特定蛋白质结构域中的丝氨酸或苏氨酸残基上。α-岩藻糖基化蛋白在多种生物学事件中发挥关键作用，并具有重要的治疗价值，其中研究最多的是Notch受体和ADAMTS蛋白。α-岩藻糖聚糖调节它们所修饰蛋白质的功能，并与包括癌症在内的各种疾病密切相关。在哺乳动物中，除了有充分文献记载的蛋白质α-岩藻糖基转移酶（POFUT）1介导的表皮生长因子样（EGF）重复序列的α-岩藻糖基化和POFUT2介导的血小板反应蛋白1型重复序列（TSR）的α-岩藻糖基化外，最近还在弹性蛋白微原纤维界面（EMI）结构域上发现了一种新型的α-岩藻糖基化，由POFUT3和POFUT4（以前称为FUT10和FUT11）介导。在这篇综述中，我们概述了目前对α-岩藻糖基化的认识，整合了最新的研究结果，并特别关注其生物学功能和分子机制。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e08e/11990869/341add2dab31/molecules-30-01470-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e08e/11990869/f20935f7274f/molecules-30-01470-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e08e/11990869/0bd7b7b3e2c8/molecules-30-01470-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e08e/11990869/55a0f9d8c73c/molecules-30-01470-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e08e/11990869/f52dda321249/molecules-30-01470-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e08e/11990869/6106d144a916/molecules-30-01470-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e08e/11990869/341add2dab31/molecules-30-01470-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e08e/11990869/f20935f7274f/molecules-30-01470-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e08e/11990869/0bd7b7b3e2c8/molecules-30-01470-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e08e/11990869/55a0f9d8c73c/molecules-30-01470-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e08e/11990869/f52dda321249/molecules-30-01470-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e08e/11990869/6106d144a916/molecules-30-01470-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e08e/11990869/341add2dab31/molecules-30-01470-g002.jpg

相似文献

[1]
Protein -Fucosyltransferases: Biological Functions and Molecular Mechanisms in Mammals.

Molecules. 2025-3-26

[2]
FUT10 and FUT11 are protein O-fucosyltransferases that modify protein EMI domains.

Nat Chem Biol. 2025-4

[3]
POFUT1-mediated O-fucosylation of glycoproteins expressed in the baculovirus Sf9 insect cell expression system.

J Biotechnol. 2024-1-10

[4]
6-alkynyl fucose is a bioorthogonal analog for O-fucosylation of epidermal growth factor-like repeats and thrombospondin type-1 repeats by protein O-fucosyltransferases 1 and 2.

Glycobiology. 2012-10-8

[5]
Analysis of endogenous NOTCH1 from POFUT1 S162L patient fibroblasts reveals the importance of the O-fucose modification on EGF12 in human development.

Glycobiology. 2024-6-22

[6]
Two distinct pathways for O-fucosylation of epidermal growth factor-like or thrombospondin type 1 repeats.

J Biol Chem. 2006-4-7

[7]
Genetic Diseases of Fucosylation: Insights from Model Organisms.

Genes (Basel). 2025-7-3

[8]
Structure of human POFUT2: insights into thrombospondin type 1 repeat fold and O-fucosylation.

EMBO J. 2012-7-18

[9]
A perspective on structural and mechanistic aspects of protein O-fucosylation.

Acta Crystallogr F Struct Biol Commun. 2018-8-1

[10]
Protein O-fucosylation: structure and function.

Curr Opin Struct Biol. 2019-1-26

引用本文的文献

[1]
F-type lectins: Structural and functional aspects, and potential biomedical applications.

BBA Adv. 2025-6-14

本文引用的文献

[1]
FUT10 and FUT11 are protein O-fucosyltransferases that modify protein EMI domains.

Nat Chem Biol. 2025-4

[2]
FUT11 expression in gastric cancer: its prognostic significance and role in immune regulation.

Discov Oncol. 2024-6-28

[3]
Integrative analysis of Lunatic Fringe variants associated with spondylocostal dysostosis type-III.

FASEB J. 2024-7-15

[4]
A metabolic inhibitor blocks cellular fucosylation and enables production of afucosylated antibodies.

Proc Natl Acad Sci U S A. 2024-7-2

[5]
Poglut2/3 double knockout in mice results in neonatal lethality with reduced levels of fibrillin in lung tissues.

J Biol Chem. 2024-7

[6]
Identification of a novel LFNG variant in a Chinese fetus with spondylocostal dysostosis and a systematic review.

J Hum Genet. 2024-7

[7]
In vivo evidence for GDP-fucose transport in the absence of transporter SLC35C1 and putative transporter SLC35C2.

J Biol Chem. 2023-12

[8]
Analysis of the Healthy Platelet Proteome Identifies a New Form of Domain-Specific O-Fucosylation.

Mol Cell Proteomics. 2024-2

[9]
A form of inherited hyperferritinemia associated with bi-allelic pathogenic variants of STAB1.

Am J Hum Genet. 2023-8-3

[10]
Knockdown of FUT11 inhibits the progression of gastric cancer via the PI3K/AKT pathway.

Heliyon. 2023-7-7

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